Hybrid Bilayers on Solid Supports

Valincius et al. used NR and ex situ electrochemical impedance spectroscopy to study the effect of amyloid (J-pephde insertion on supported hpid bilayers [60]. It has been speculated that the interaction between these oligomeric proteins and bilayer membranes plays an important role in the aggregation and protein misfold-ing that leads to various neurodegenerahve diseases including Alzehimer s and Parkinson s diseases [61]. Using a variety of solvent and phospholipid contrasts, including the use of perdeuterated phosphohpids, NR demonstrated that amyloid P-peptides inserted into hpid bilayers tethered to a gold-modified silicon substrate. 

The NR data revealed that the protein fully inserts into the hydrophobic core, disrupting both hpid leaflets but does not lead to significant disruphon of the head group region as determined by the absence of increased water content in the SLD profiles. This information was vital for explaining the results of ex situ impedance spectroscopy and modeling the increased ion transport capabilities of the supported membranes in the presence of amyloid [3-pephdes. 

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